Live cell NMR

Annual Review of Biophysics

Volumn 43, Issue 1, 2014, Pages 171-192

  Freedberg, Darón I ^a   Selenko, Philipp ^b  

^a CENTER FOR BIOLOGICS EVALUATION AND RESEARCH   (United States)

^b LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE   (Germany)

Author keywords

Excluded volume; In cell EPR; In cell NMR; Macromolecular crowding; On cell NMR; Soft interactions

Indexed keywords

CELL PROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; DNA; RECOMBINANT PROTEIN; RNA;

ARTICLE; CELL MATURATION; CELLS; DYNAMICS; ELECTRON SPIN RESONANCE; ESCHERICHIA COLI; EUKARYOTE; HEK293 CELL LINE; HELA CELL LINE; HUMAN; IN CELL ELECTRON PARAMAGNETIC RESONANCE; IN CELL NUCLEAR MAGNETIC RESONANCE; INSECT; LIVE CELL NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; METAL BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROKARYOTE; PROTEIN STABILITY; PROTEIN STRUCTURE; SOLID STATE; SOLID STATE IN CELL NUCLEAR MAGNETIC RESONANCE; SOLID STATE ON CELL NUCLEAR MAGNETIC RESONANCE; SOLUTION STATE IN CELL NUCLEAR MAGNETIC RESONANCE; SOLUTION STATE ON CELL NUCLEAR MAGNETIC RESONANCE; XENOPUS LAEVIS; YEAST;

EXCLUDED VOLUME; IN-CELL EPR; IN-CELL NMR; MACROMOLECULAR CROWDING; ON-CELL NMR; SOFT INTERACTIONS;

ANIMALS; BACTERIA; EUKARYOTIC CELLS; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS;

EID: 84901983051     PISSN: 1936122X     EISSN: 19361238     Source Type: Book Series    
DOI: 10.1146/annurev-biophys-051013-023136     Document Type: Article

References (110)

1. Amata I, Maffei M, Igea A, Gay M, Vilaseca M, et al. 2013. Multi-phosphorylation of the intrinsically disordered unique domain of c-Src studied by in-cell and real-time NMR spectroscopy. ChemBioChem. 14:1820-277
2. Arnesano F, Banci L, Bertini I, Felli IC, Losacco M, Natile G. 2011. Probing the interaction of cisplatin with the human copper chaperone Atox1 by solution and in-cell NMR spectroscopy. J. Am. Chem. Soc. 133:18361-699
3. Assadi-Porter FM, Tonelli M, Maillet E, Hallenga K, Benard O, et al. 2008. Direct NMR detection of the binding of functional ligands to the human sweet receptor, a heterodimeric family 3 GPCR. J. Am. Chem. Soc. 130:7212-133
4. Augustus AM, Reardon PN, Spicer LD. 2009. MetJ repressor interactions with DNA probed by in-cell NMR. Proc. Natl. Acad. Sci. USA 106:5065-699
5. Azarkh M, Okle O, Eyring P, Dietrich DR, DrescherM. 2011. Evaluation of spin labels for in-cell EPR by analysis of nitroxide reduction in cell extract of Xenopus laevis oocytes. J. Magn. Reson. 212:450-544
6. Azarkh M, Okle O, Singh V, Seemann IT, Hartig JS, et al. 2011. Long-range distance determination in a DNA model system inside Xenopus laevis oocytes by in-cell spin-label EPR. ChemBioChem 12:1992-955
7. Azarkh M, Singh V, Okle O, Dietrich DR, Hartig JS, Drescher M. 2012. Intracellular conformations of human telomeric quadruplexes studied by electron paramagnetic resonance spectroscopy. ChemPhysChem 13:1444-477
8. Azarkh M, Singh V, Okle O, Seemann IT, Dietrich DR, et al. 2013. Site-directed spin-labeling of nucleotides and the use of in-cell EPR to determine long-range distances in a biologically relevant environment. Nat. Protoc. 8:131-477
9. Azurmendi HF, Vionnet J, Wrightson L, Trinh LB, Shiloach J, Freedberg DI. 2007. Extracellular structure of polysialic acid explored by on cell solution NMR. Proc. Natl. Acad. Sci. USA 104:11557-611
10. Banci L, Barbieri L, Bertini I, Cantini F, Luchinat E. 2011. In-cellNMRin E. Coli to monitormaturation steps of hSOD1. PLoS ONE 6:e235611
11. Banci L, Barbieri L, Bertini I, Luchinat E, Secci E, et al. 2013. Atomic-resolution monitoring of protein maturation in live human cells by NMR. Nat. Chem. Biol. 9:297-999
12. Banci L, Barbieri L, Luchinat E, Secci E. 2013. Visualization of redox-controlled protein fold in living cells. Chem. Biol. 20:747-52
13. Barb AW, Freedberg DI, Battistel MD, Prestegard JH. 2011. NMR detection and characterization of sialylated glycoproteins and cell surface polysaccharides. J. Biomol. NMR 51:163-711
14. Barnes CO, Monteith WB, Pielak GJ. 2011. Internal and global protein motion assessed with a fusion construct and in-cell NMR spectroscopy. ChemBioChem 12:390-911
15. Barnes CO, Pielak GJ. 2011. In-cell protein NMR and protein leakage. Proteins 79:347-511
16. Benton LA, Smith AE, Young GB, Pielak GJ. 2012. Unexpected effects of macromolecular crowding on protein stability. Biochemistry 51:9773-755
17. Bertrand K, Reverdatto S, Burz DS, Zitomer R, Shekhtman A. 2012. Structure of proteins in eukaryotic compartments. J. Am. Chem. Soc. 134:12798-8066
18. Bodart J-F, Wieruszeski J-M, Amniai L, Leroy A, Landrieu I, et al. 2008. NMR observation of Tau in Xenopus oocytes. J. Magn. Reson. 192:252-577
19. Burz DS,Dutta K, CowburnD, Shekhtman A. 2006. Mapping structural interactions using in-cellNMR spectroscopy (STINT-NMR). Nat. Methods 3:91-933
20. Claasen B, Axmann M, Meinecke R, Meyer B. 2005. Direct observation of ligand binding to membrane proteins in living cells by a saturation transfer double difference (STDD) NMR spectroscopy method shows a significantly higher affinity of integrin IIb3 in native platelets than in liposomes. J. Am. Chem. Soc. 127:916-199
21. Costa JL, Dobson CM,KirkKL, Poulsen FM, Valeri CR, Vecchione JJ. 1979. Studies of human platelets by 19F and 31P NMR. FEBS Lett. 99:141-466
22. Costa JL, Dobson CM, Kirk KL, Poulsen FM, Valeri CR, Vecchione JJ. 1980. Nuclear magnetic resonance studies of blood platelets. Philos. Trans. R. Soc. Lond. B 289:413-233
23. Crowley PB, Chow E, Papkovskaia T. 2011. Protein interactions in the Escherichia coli cytosol: an impediment to in-cell NMR spectroscopy. ChemBioChem 12:1043-488
24. Crowley PB, Kyne C, Monteith WB. 2012. Simple and inexpensive incorporation of 19F-tryptophan for protein NMR spectroscopy. Chem. Commun. 48:10681-833
25. Curtis-Fisk J, Spencer RM,Weliky DP. 2008. Native conformation at specific residues in recombinant inclusion body protein in whole cells determined with solid-state NMR spectroscopy. J. Am. Chem. Soc. 130:12568-699
26. Danielsson J, Inomata K, Murayama S, Tochio H, Lang L, et al. 2013. Pruning the ALS-associated protein SOD1 for in-cell NMR. J. Am. Chem. Soc. 135:10266-699
27. Deeds EJ, Ashenberg O, Shakhnovich EI. 2006. A simple physical model for scaling in protein-protein interaction networks. Proc. Natl. Acad. Sci. USA 103:311-166
28. Deszo EL, Steenbergen SM, Freedberg DI, Vimr ER. 2005. Escherichia coli K1 polysialic acid O-acetyltransferase gene, neuO, and the mechanism of capsule form variation involving a mobile contingency locus. Proc. Natl. Acad. Sci. USA 102:5564-699
29. Dick-Pérez M, Zhang Y, Hayes J, Salazar A, Zabotina OA, Hong M. 2011. Structure and interactions of plant cell-wall polysaccharides by two-and three-dimensional magic-angle-spinning solid-state NMR. Biochemistry 50:989-1000
30. Ellis RJ. 2001. Macromolecular crowding: an important but neglected aspect of the intracellular environment. Curr. Opin. Struct. Biol. 11:114-199
31. Ellis RJ. 2001. Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci. 26:597-6044
32. Feig M, Sugita Y. 2012. Variable interactions between protein crowders and biomolecular solutes are important in understanding cellular crowding. J. Phys. Chem. B 116:599-6055
33. Fu R, Wang X, Li C, Santiago-Miranda AN, Pielak GJ, Tian F. 2011. In situ structural characterization of a recombinant protein in native Escherichia coli membranes with solid-state magic-angle-spinning NMR. J. Am. Chem. Soc. 133:12370-733
34. Hamatsu J, O'Donovan D, Tanaka T, Shirai T, Hourai Y, et al. 2013. High-resolution heteronuclear multidimensional NMR of proteins in living insect cells using a baculovirus protein expression system. J. Am. Chem. Soc. 135:1688-911
35. Hammill JT, Miyake-Stoner S, Hazen JL, Jackson JC, Mehl RA. 2007. Preparation of site-specifically labeled fluorinated proteins for 19F-NMR structural characterization. Nat. Protoc. 2:2601-77
36. Hänsel R, Foldynová-Trantíková S, DötschV, Tranték L. 2013. Investigation of quadruplex structure under physiological conditions using in-cell NMR. Top. Curr. Chem. 330:47-655
37. Hänsel R, Foldynová-Trantíková S, Löhr F, Buck J, Bongartz E, et al. 2009. Evaluation of parameters critical for observing nucleic acids inside living Xenopus laevis oocytes by in-cell NMR spectroscopy. J. Am. Chem. Soc. 131:15761-688
38. Hansel R, Lohr F, Foldynová-Trant́rková S, Bamberg E, Trant́rek L, Dotsch V. 2011. The parallel G-quadruplex structure of vertebrate telomeric repeat sequences is not the preferred folding topology under physiological conditions. Nucleic Acids Res. 39:5768-755
39. Hansel R, Löhr F, Tranték L, Dötsch V. 2013. High-resolution insight into G-overhang architecture. J. Am. Chem. Soc. 135:2816-244
40. HeoM,Maslov S, Shakhnovich E. 2011. Topology of protein interaction network shapes protein abundances and strengths of their functional and nonspecific interactions. Proc.Natl. Acad. Sci. USA 108:4258-633
41. Holder IT, Drescher M, Hartig JS. 2013. Structural characterization of quadruplex DNA with in-cell EPR approaches. Bioorganic Med. Chem. 21:6156-611
42. Igarashi R, Sakai T,HaraH, Tenno T, Tanaka T, et al. 2010. Distance determination in proteins inside Xenopus laevis oocytes by double electron-electron resonance experiments. J. Am. Chem. Soc. 132:8228-299
43. Inomata K, Ohno A, Tochio H, Isogai S, Tenno T, et al. 2009. High-resolution multi-dimensional NMR spectroscopy of proteins in human cells. Nature 458:106-99
44. Ito Y, Selenko P. 2010. Cellular structural biology. Curr. Opin. Struct. Biol. 20:640-488
45. Jachymek W, Niedziela T, Petersson C, Lugowski C, Czaja J, Kenne L. 1999. Structures of the O-specific polysaccharides from Yokenella regensburgei (Koserella trabulsii ) strains PCM2476, 2477, 2478, and 2494: high-resolution magic-angle spinning NMR investigation of the O-specific polysaccharides in native lipopolysaccharides and directly on the surface of living bacteria. Biochemistry 38:11788-955
46. Jackson JC, Hammill JT, Mehl RA. 2007. Site-specific incorporation of a 19F-amino acid into proteins as an NMR probe for characterizing protein structure and reactivity. J. Am. Chem. Soc. 129:1160-666
47. Jacso T, Franks WT, Rose H, Fink U, Broecker J, et al. 2012. Characterization of membrane proteins in isolated native cellular membranes by dynamic nuclear polarization solid-state NMR spectroscopy without purification and reconstitution. Angew. Chem. Int. Ed. 51:432-355
48. Kern T, Giffard M, Hediger S, Amoroso A, Giustini C, et al. 2010. Dynamics characterization of fully hydrated bacterial cell walls by solid-state NMR: evidence for cooperative binding of metal ions. J. Am. Chem. Soc. 132:10911-199
49. Kern T, Hediger S, Müller P, Giustini C, Joris B, et al. 2008. Toward the characterization of peptidoglycan structure and protein-peptidoglycan interactions by solid-stateNMR spectroscopy. J. Am. Chem. Soc. 130:5618-199
50. Kim SJ, Schaefer J. 2008. Hydrophobic side-chain length determines activity and conformational heterogeneity of a vancomycin derivative bound to the cell wall of Staphylococcus aureus. Biochemistry 47:10155-611
51. Kim SJ, Singh M, Schaefer J. 2009. Oritavancin binds to isolated protoplast membranes but not intact protoplasts of Staphylococcus aureus. J. Mol. Biol. 391:414-255
52. Krstić I, Hänsel R, Romainczyk O, Engels JW, Dötsch V, Prisner TF. 2011. Long-range distance measurements on nucleic acids in cells by pulsed EPR spectroscopy. Angew. Chem. Int. Ed. 50:5070-744
53. Kubo S, Nishida N, Udagawa Y, Takarada O, Ogino S, Shimada I. 2013. A gel-encapsulated bioreactor system for NMR studies of protein-protein interactions in living mammalian cells. Angew. Chem. Int. Ed. 52:1208-111
54. Latham MP, Kay LE. 2012. Is buffer a good proxy for a crowded cell-like environment? A comparative NMR study of calmodulin side-chain dynamics in buffer and E. Coli lysate. PLoS ONE 7:e482266
55. Latham MP, Kay LE. 2013. Probing nonspecific interactions of Ca2+-calmodulin in E. Coli lysate. J. Biomol. NMR 55:239-477
56. Li C, Liu M. 2013. Protein dynamics in living cells studied by in-cell NMR spectroscopy. FEBS Lett. 587:1008-111
57. Li C, Lutz EA, Slade KM, Ruf RA, Wang GF, Pielak GJ. 2009. 19F NMR studies of α-synuclein conformation and fibrillation. Biochemistry 48:8578-844
58. Li C, Wang G-F, Wang Y, Creager-Allen R, Lutz EA, et al. 2010. Protein 19F NMR in Escherichia coli. J. Am. Chem. Soc. 132:321-277
59. Linden AH, Lange S, Franks WT, Akbey U, Specker E, et al. 2011. Neurotoxin II bound to acetylcholine receptors in native membranes studied by dynamic nuclear polarizationNMR. J. Am. Chem. Soc. 133:19266-699
60. Link AJ, Robison K, Church GM. 1997. Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18:1259-3133
61. Liu CC, Schultz PG. 2010. Adding new chemistries to the genetic code. Annu. Rev. Biochem. 79:413-444
62. Liu JJ, Horst R, Katritch V, Stevens RC, Wuthrich K. 2012. Biased signaling pathways in β2-adrenergic receptor characterized by 19F-NMR. Science 335:1106-100
63. Maldonado AY, Burz DS, Shekhtman A. 2011. In-cell NMR spectroscopy. Prog. Nucl. Magn. Reson. Spectrosc. 59:197-2122
64. Mari S, Invernizzi C, Spitaleri A, Alberici L, Ghitti M, et al. 2010. 2D TR-NOESY experiments interrogate and rank ligand-receptor interactions in living human cancer cells. Angew. Chem. Int. Ed. 49:1071-744
65. Mari S, Serrano-Gómez D, Cañada FJ, Corbí AL, Jiménez-Barbero J. 2004. 1D saturation transfer difference NMR experiments on living cells: the DC-SIGN/oligomannose interaction. Angew. Chem. Int. Ed. 44:296-988
66. Miklos AC, Li C, Sharaf NG, Pielak GJ. 2010. Volume exclusion and soft interaction effects on protein stability under crowded conditions. Biochemistry 49:6984-911
67. Miklos AC, Li C, Sorrell CD, Lyon LA, Pielak GJ. 2011. An upper limit for macromolecular crowding effects. BMC Biophys. 4:133
68. Miklos AC, SarkarM,Wang Y, Pielak GJ. 2011. Protein crowding tunes protein stability. J. Am. Chem. Soc. 133:7116-200
69. Minton AP. 2000. Implications of macromolecular crowding for protein assembly. Curr. Opin. Struct. Biol. 10:34-399
70. Minton AP. 2001. The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J. Biol. Chem. 276:10577-800
71. Minton AP. 2013. Quantitative assessment of the relative contributions of steric repulsion and chemical interactions to macromolecular crowding. Biopolymers 99:239-444
72. Ogino S, Kubo S, Umemoto R, Huang S, Nishida N, Shimada I. 2009. Observation of NMR signals from proteins introduced into living mammalian cells by reversible membrane permeabilization using a pore-forming toxin, streptolysin O. J. Am. Chem. Soc. 131:10834-355
73. Patti GJ, Kim SJ, Yu T-Y, Dietrich E, Tanaka KSE, et al. 2009. Vancomycin and oritavancin have different modes of action in Enterococcus faecium. J. Mol. Biol. 392:1178-911
74. Pielak GJ, Li C, Miklos AC, Schlesinger AP, Slade KM, et al. 2009. Protein nuclear magnetic resonance under physiological conditions. Biochemistry 48:226-344
75. Pielak GJ, Tian F. 2012. Membrane proteins, magic-angle spinning, and in-cell NMR. Proc. Natl. Acad. Sci. USA 109:4715-166
76. Potenza D, Belvisi L. 2008. Transferred-NOE NMR experiments on intact human platelets: receptorbound conformation of RGD-peptide mimics. Org. Biomol. Chem. 6:258-622
77. Potenza D, Vasile F, Belvisi L, Civera M, Araldi EMV. 2011. STD and trNOESY NMR study of receptor-ligand interactions in living cancer cells. ChemBioChem 12:695-999
78. Reckel S, Lopez JJ, Löhr F, Glaubitz C, Dötsch V. 2012. In-cell solid-state NMR as a tool to study proteins in large complexes. ChemBioChem 13:534-377
79. Renault M, Cukkemane A, Baldus M. 2010. Solid-state NMR spectroscopy on complex biomolecules. Angew. Chem. Int. Ed. 49:8346-577
80. RenaultM, Pawsey S, Bos MP, Koers EJ,NandD, et al. 2012. Solid-stateNMRspectroscopy on cellular preparations enhanced by dynamic nuclear polarization. Angew. Chem. Int. Ed. 51:2998-30011
81. Renault M, Tommassen-van Boxtel R, BosMP, Post JA, Tommassen J, BaldusM. 2012. Cellular solid-state nuclear magnetic resonance spectroscopy. Proc. Natl. Acad. Sci. USA 109:4863-688
82. Sakai T, Tochio H, Inomata K, Sasaki Y, Tenno T, et al. 2007. Fluoroscopic assessment of protein leakage during Xenopus oocytes in-cell NMR experiment by co-injected EGFP. Anal. Biochem. 371:247-499
83. Sakai T, TochioH, Tenno T, Ito Y, Kokubo T, et al. 2006. In-cellNMRspectroscopy of proteins inside Xenopus laevis oocytes. J. Biomol. NMR 36:179-888
84. Sarkar M, Li C, Pielak GJ. 2013. Soft interactions and crowding. Biophys. Rev. 1:1-88
85. Schlesinger AP, Wang Y, Tadeo X, Millet O, Pielak GJ. 2011. Macromolecular crowding fails to fold a globular protein in cells. J. Am. Chem. Soc. 133:8082-855
86. Selenko P, Frueh DP, Elsaesser SJ, Haas W, Gygi SP, Wagner G. 2008. In situ observation of protein phosphorylation by high-resolution NMR spectroscopy. Nat. Struct. Mol. Biol. 15:321-299
87. Selenko P, Serber Z, Gadea B, Ruderman J, Wagner G. 2006. Quantitative NMR analysis of the protein G B1 domain in Xenopus laevis egg extracts and intact oocytes. Proc. Natl. Acad. Sci. USA 103:11904-99
88. Serber Z, Corsini L, Durst F, Dötsch V. 2005. In-cell NMR spectroscopy. Methods Enzymol. 394:17-411
89. Serber Z, Keatinge-Clay AT, Ledwidge R, Kelly AE, Miller SM, Dötsch V. 2001. High-resolution macromolecular NMR spectroscopy inside living cells. J. Am. Chem. Soc. 123:2446-477
90. Serber Z, Ledwidge R, Miller SM, Dötsch V. 2001. Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy. J. Am. Chem. Soc. 123:8895-9011
91. Serber Z, Selenko P, Hänsel R, Reckel S, Löhr F, et al. 2006. Investigating macromolecules inside cultured and injected cells by in-cell NMR spectroscopy. Nat. Protoc. 1:2701-99
92. Sharaf NG, Barnes CO, Charlton LM, Young GB, Pielak GJ. 2010. A bioreactor for in-cell protein NMR. J. Magn. Reson. 202:140-466
93. Shi P, Li D, Chen H, Xiong Y,Wang Y, Tian C. 2012. In situ 19F NMR studies of an E. Coli membrane protein. Protein Sci. 21:596-6000
94. Shulman RG,Ogawa S, Mayer A,Castillo CL. 1973. High-resolution protonNMRstudies of low affinity hemoglobins. Ann. N.Y. Acad. Sci. 222:9-200
95. Singh V, Azarkh M, Exner TE, Hartig JS, Drescher M. 2009. Human telomeric quadruplex conformations studied by pulsed EPR. Angew. Chem. Int. Ed. 48:9728-300
96. SladeKM, Baker R,ChuaM,ThompsonNL, Pielak GJ. 2009. Effects of recombinant protein expression on green fluorescent protein diffusion in Escherichia coli. Biochemistry 48:5083-899
97. Snyder GK. 1977. Blood corpuscles and blood hemoglobins: a possible example of coevolution. Science 195:412-133
98. Spitzer J, Poolman B. 2009. The role of biomacromolecular crowding, ionic strength, and physicochemical gradients in the complexities of life's emergence. Microbiol. Mol. Biol. Rev. 73:371-888
99. Tadeo X, López-Mández B, Trigueros T, Laín A, Castano D, Millet O. 2009. Structural basis for the aminoacid composition of proteins from halophilic archea. PLoS Biol. 7:e10002577
100. Takahashi H, Ayala I, Bardet M, De Paëpe G, Simorre J-P, Hediger S. 2013. Solid-state NMR on bacterial cells: selective cell wall signal enhancement and resolution improvement using dynamic nuclear polarization. J. Am. Chem. Soc. 135:5105-100
101. Wang Q, Zhuravleva A, Gierasch LM. 2011. Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy. Biochemistry 50:9225-366
102. WangY, Sarkar M, SmithAE, KroisAS, Pielak GJ. 2012. Macromolecular crowding and protein stability. J. Am. Chem. Soc. 134:16614-188
103. Wasmer C, Benkemoun L, Sabaté R, Steinmetz MO, Coulary-Salin B, et al. 2009. Solid-state NMR spectroscopy reveals that E. Coli inclusion bodies of HET-s(218-289) are amyloids. Angew. Chem. Int. Ed. 48:4858-600
104. Wieruszeski JM, Bohin A, Bohin JP, Lippens G. 2001. In vivo detection of the cyclic osmoregulated periplasmic glucan of Ralstonia solanacearum by high-resolution magic angle spinning NMR. J. Magn. Reson. 151:118-233
105. Ye Y, Liu X, Zhang Z, Wu Q, Jiang B, et al. 2013. 19F NMR spectroscopy as a probe of cytoplasmic viscosity and weak protein interactions in living cells. Chem. Eur. J. 19:12705-100
106. Zandomeneghi G, Ilg K, Aebi M, Meier BH. 2012. On-cellMAS NMR: physiological clues from living cells. J. Am. Chem. Soc. 134:17513-199
107. Zhong J, Frases S,Wang H, Casadevall A, Stark RE. 2008. Following fungal melanin biosynthesis with solid-state NMR: biopolymer molecular structures and possible connections to cell-wall polysaccharides. Biochemistry 47:4701-100
108. Zhou X, Cegelski L. 2012. Nutrient-dependent structural changes in S. aureus peptidoglycan revealed by solid-state NMR spectroscopy. Biochemistry 51:8143-533
109. Zigoneanu IG, Pielak GJ. 2012. Interaction of α-synuclein and a cell penetrating fusion peptide with higher eukaryotic cell membranes assessed by 19F NMR. Mol. Pharm. 9:1024-299
110. Zigoneanu IG, Yang YJ, Krois AS, Haque E, Pielak GJ. 2012. Interaction of α-synuclein with vesicles that mimic mitochondrial membranes. Biochim. Biophys. Acta 1818:512-199